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The Cellular Prion Protein Interacts with the Tissue Non-Specific Alkaline Phosphatase in Membrane Microdomains of Bioaminergic Neuronal Cells

Figure 10

Diagram depicting possible implications of a PrPC-TNAP association in membrane microdomains of neuronal cells.

PrPC and TNAP are GPI-anchored membrane proteins, which majorly reside in rafts. Both have been described to interact with ECM proteins [16], [53], [54] and to participate to cell signaling events. PrPC can instruct downstream signaling events, including ERK and CREB activation, by mobilizing a Cav/Fyn complex on neurites [3], [22][24]. In addition, it modulates the coupling of 5-HT receptors, with specific impact according to G protein-dependent pathway [25]. The TNAP ectophosphatase may have different substrates. (i) By promoting PLP hydrolysis it contributes to the regulation of neurotransmitter synthesis [33]. (ii) Its nucleotidase activity may have implications for purinergic signaling [30], [46][48]. (iii) TNAP may be active on phosphoproteins notably of the cell surface [51], [52]. The identification of phospho-laminin as a TNAP substrate uncovers a novel role of this ectoenzyme in the regulation of ECM molecules. Laminin and the laminin receptor are important components of the perineural net (PN) and are known partners of PrPC. The interplay between PrPC, laminin and TNAP within multiprotein complexes may have implications for neuronal functions (survival, homeostasis, plasticity).

Figure 10

doi: https://doi.org/10.1371/journal.pone.0006497.g010